Information on EC 3.13.1.3 - 2'-hydroxybiphenyl-2-sulfinate desulfinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.13.1.3
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RECOMMENDED NAME
GeneOntology No.
2'-hydroxybiphenyl-2-sulfinate desulfinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2'-hydroxybiphenyl-2-sulfinate + H2O = 2-hydroxybiphenyl + sulfite
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
desulfination
oxidation
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-
-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dibenzothiophene desulfurization
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SYSTEMATIC NAME
IUBMB Comments
2'-hydroxybiphenyl-2-sulfinate sulfohydrolase
The enzyme from Rhodococcus sp. strain IGTS8 is encoded by the plasmid-encoded dibenzothiophene-desulfurization (dsz) operon. The enzyme has a narrow substrate specificity with biphenyl-2-sulfinate being the only other substrate known to date [2].
CAS REGISTRY NUMBER
COMMENTARY hide
198154-06-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain A11-2
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Manually annotated by BRENDA team
strain A11-2
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Manually annotated by BRENDA team
strain CECT5279, gene dszB
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Manually annotated by BRENDA team
strain CECT5279, gene dszB
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Manually annotated by BRENDA team
strain IGTS8, ATCC 53968
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Manually annotated by BRENDA team
strain IGT8, ATCC 53968
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Manually annotated by BRENDA team
IGTS8
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
show the reaction diagram
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
show the reaction diagram
2-(2'-hydroxyphenyl)ethene-1-sulfinate + H2O
o-hydroxystyrene + sulfite
show the reaction diagram
2-(2-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
show the reaction diagram
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
show the reaction diagram
2-phenylbenzenesulfinate + H2O
biphenyl + sulfite
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2'-hydroxybiphenyl-2-sulfinate + H2O
2-hydroxybiphenyl + sulfite
show the reaction diagram
2-(2'-hydroxyphenyl)benzenesulfinate + H2O
2-hydroxybiphenyl + sulfite
show the reaction diagram
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no metal ions required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-Dihydroxybiphenyl
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competitive
2,3-Dihydroxybiphenyl
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competitive
2-Hydroxybiphenyl
Ag+
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strong inhibition at 1 mM
Co2+
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18% inhibition at 0.1 mM
Hg2+
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strong inhibition at 1 mM
iodoacetic acid
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95% inhibition at 1 mM
Mn2+
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71% inhibition at 1 mM
N-bromosuccimide
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complete inhibition at 0.01 mM after 10 min
N-ethylmaleimide
Ni2+
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24% inhibition at 1 mM
o-hydroxystyrene
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product inhibition, 80% inhibition at 5 mM, the OH-group is important for the inhibitory effect
p-chloromercuribenzoate
phenylglyoxal hydrate
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19% inhibition at 0.01 mM after 10 min
pyridoxal-5-phosphate
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38% inhibition at 0.01 mM after 10 min
Tetranitromethane
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complete inhibition at 0.01 mM after 10 min
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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10% activation at 0.1 mM
Mg2+
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1.23fold activation at 1 mM
additional information
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no activation by metal ions
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0056 - 0.0556
2'-hydroxybiphenyl-2-sulfinate
0.0009
2-(2'-hydroxyphenyl)benzenesulfinate
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pH 7.4, 35°C
0.33
2-(2-hydroxyphenyl)benzenesulfinate
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pH 7.0, 50°C
0.062
2-phenylbenzenesulfinate
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pH 7.0, 28°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
2,2'-Dihydroxybiphenyl
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pH 7.0, 28°C, recombinant enzyme
0.4
2,3-Dihydroxybiphenyl
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pH 7.0, 28°C, recombinant enzyme
0.25
2-Hydroxybiphenyl
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pH 7.0, 28°C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00046
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purified enzyme
0.139
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purified enzyme
0.18
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purified native enzyme
0.207
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purified recombinant enzyme
8.3
mutant Y63K, pH 7.0, 28°C
21
mutant Q65H, pH 7.0, 28°C
26.8
wild-type, pH 7.0, 28°C
29.2
mutant Y63W, pH 7.0, 28°C
34.1
mutant Y63F/Q65H, pH 7.0, 28°C
43
mutant Y63F, pH 7.0, 28°C
49.1
mutant Y63A, pH 7.0, 28°C
61.1
mutant Y63S, pH 7.0, 28°C
additional information
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desulfurization activity in strain CECT5279 over time in vivo
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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about, recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.4
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activity decreases sigificantly below pH 6.0 and above pH 8.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
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rapid loss of activity at temperatures higher or lower than the optimum
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 5.9
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isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
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gel filtration
39000
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1 * 39000, SDS-PAGE
43000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of DszB and an inactive mutant of DszB in complex with substrate at resolution of 1.8 A or better
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DszB and DszB C27S mutant complexed with biphenyl-2-sulfinic acid are crystallized. The crystals of DszB belong to the orthorhombic P2(1)2(1)2(1) space group, with unit-cell parameters a = 36.7 A, b = 82.6 A, c = 139.6 A, and contain one molecule of DszB in the asymmetric unit. Crystals of DszB C27S complexed with biphenyl-2-sulfinic acid belong to space group C2 with unit-cell parameters a = 153.4 A, b = 45.9 A, c = 112.9 A, beta = 115.93°
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28
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recombinant enzyme, stable
30
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recombinant enzyme, rapid loss of activity above, inactivation after 4 h
35
30 min, wild-type, almost complete loss of activity, mutant Y63F/Q65H, 90% residual activity
40
30 min,mutant Y63F/Q65H, 90% residual activity
55
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30 min, stable up to
60
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rapid loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from strain A11-2 63fold
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recombinant 7.8fold from Escherichia coli, and native from strain KA2-5-1 160fold, to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene dszB, DszB expression pattern in Pseudomonas putida strain CECT5279
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gene dszB, organized in the dsz operon, DNA and amino acid sequence determination and analysis, genetic organization and expression analysis, recombinant expression in recombinant Rhodococcus erythropolis strain CGMCC 4.1491, that is dsz-deficient
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gene dszZ, DNA sequence determination, cooverexpression in Escherichia coli with chaperonin genes groEL and groES at 25°C
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gene tdsB, DNA sequence determination, overexpression in Escherichia coli BL21 (DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C26S
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site-directed mutagenesis of the only cysteine residue results in an completely inactive mutant
H60Q
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mutation causes an 17fold reduction in the specific activity
Q65H
increase in thermostability, decrease in catalytic activity
R70I
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inactive mutant mostly exists in the insoluble fraction of the cell extract
R70K
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inactive mutant mostly exists in the insoluble fraction of the cell extract
Y63A
increase in catalytic activity
Y63F
increase in catalytic activity, similar thermostability as wild-type
Y63F/Q65H
increase in thermostability without loss of catalytic activity or affinity for substrate
Y63K
decrease in activity
Y63S
affinity for the substrate is about 7-fold lower than that of the wild-type enzyme
Y63W
activity similar to wild-type
C26S
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site-directed mutagenesis of the only cysteine residue results in an completely inactive mutant
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Q65H
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increase in thermostability, decrease in catalytic activity
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Y63A
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increase in catalytic activity
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Y63F
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increase in catalytic activity, similar thermostability as wild-type
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Y63S
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affinity for the substrate is about 7-fold lower than that of the wild-type enzyme
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Y63W
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activity similar to wild-type
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
energy production
additional information